LYPLA3

Protein-coding gene in the species Homo sapiens
PLA2G15
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

4X90, 4X91, 4X92, 4X93, 4X94, 4X95, 4X97

Identifiers
AliasesPLA2G15, ACS, GXVPLA2, LLPL, LPLA2, LYPLA3, phospholipase A2 group XV
External IDsOMIM: 609362; MGI: 2178076; HomoloGene: 8200; GeneCards: PLA2G15; OMA:PLA2G15 - orthologs
Gene location (Human)
Chromosome 16 (human)
Chr.Chromosome 16 (human)[1]
Chromosome 16 (human)
Genomic location for PLA2G15
Genomic location for PLA2G15
Band16q22.1Start68,245,304 bp[1]
End68,261,058 bp[1]
Gene location (Mouse)
Chromosome 8 (mouse)
Chr.Chromosome 8 (mouse)[2]
Chromosome 8 (mouse)
Genomic location for PLA2G15
Genomic location for PLA2G15
Band8|8 D3Start106,877,031 bp[2]
End106,891,347 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • gastrocnemius muscle

  • apex of heart

  • muscle of thigh

  • left ventricle

  • right auricle

  • right hemisphere of cerebellum

  • stromal cell of endometrium

  • glutes

  • right lobe of liver

  • monocyte
Top expressed in
  • stroma of bone marrow

  • secondary oocyte

  • primary oocyte

  • blastocyst

  • blastocyst

  • zygote

  • calvaria

  • morula

  • lumbar spinal ganglion

  • spleen
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • transferase activity
  • O-acyltransferase activity
  • lysophospholipase activity
  • acyltransferase activity
  • hydrolase activity
  • phospholipid binding
  • calcium-independent phospholipase A2 activity
Cellular component
  • membrane
  • mitochondrion
  • lysosome
  • extracellular exosome
  • extracellular space
  • nucleoplasm
  • intracellular membrane-bounded organelle
  • extracellular region
Biological process
  • fatty acid catabolic process
  • phosphatidylcholine catabolic process
  • ceramide metabolic process
  • lipid metabolism
  • fatty acid metabolic process
  • lipid catabolic process
  • phosphatidylethanolamine catabolic process
  • glycerophospholipid metabolic process
  • phosphatidylcholine metabolic process
  • phospholipid metabolic process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

23659

192654

Ensembl

ENSG00000103066

ENSMUSG00000031903

UniProt

Q8NCC3

Q8VEB4

RefSeq (mRNA)

NM_012320
NM_001363551

NM_133792
NM_001357319

RefSeq (protein)

NP_036452
NP_001350480

NP_598553
NP_001344248

Location (UCSC)Chr 16: 68.25 – 68.26 MbChr 8: 106.88 – 106.89 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

LYPLA3, also known as Group XV phospholipase A2, is an enzyme that in humans is encoded by the PLA2G15 gene.[5][6][7]

Lysophospholipases are enzymes that act on biological membranes to regulate the multifunctional lysophospholipids. The protein encoded by this gene hydrolyzes lysophosphatidylcholine to glycerophosphorylcholine and a free fatty acid. This enzyme is present in the plasma and thought to be associated with high-density lipoprotein. A later paper contradicts the function of this gene. It demonstrates that this gene encodes a lysosomal enzyme instead of a lysophospholipase and has both calcium-independent phospholipase A2 and transacylase activities.[7]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000103066 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000031903 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Taniyama Y, Shibata S, Kita S, Horikoshi K, Fuse H, Shirafuji H, Sumino Y, Fujino M (May 1999). "Cloning and expression of a novel lysophospholipase which structurally resembles lecithin cholesterol acyltransferase". Biochem Biophys Res Commun. 257 (1): 50–6. doi:10.1006/bbrc.1999.0411. PMID 10092508.
  6. ^ Schaloske RH, Dennis EA (Nov 2006). "The phospholipase A2 superfamily and its group numbering system". Biochim Biophys Acta. 1761 (11): 1246–59. doi:10.1016/j.bbalip.2006.07.011. PMID 16973413.
  7. ^ a b "Entrez Gene: LYPLA3 lysophospholipase 3 (lysosomal phospholipase A2)".

Further reading

  • Wang A, Dennis EA (1999). "Mammalian lysophospholipases". Biochim. Biophys. Acta. 1439 (1): 1–16. doi:10.1016/s1388-1981(99)00063-3. PMID 10395961.
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
  • Ohta T, Michel JJ, Schottelius AJ, Xiong Y (1999). "ROC1, a homolog of APC11, represents a family of cullin partners with an associated ubiquitin ligase activity". Mol. Cell. 3 (4): 535–41. doi:10.1016/S1097-2765(00)80482-7. PMID 10230407. S2CID 19371828.
  • Hiraoka M, Abe A, Shayman JA (2002). "Cloning and characterization of a lysosomal phospholipase A2, 1-O-acylceramide synthase". J. Biol. Chem. 277 (12): 10090–9. doi:10.1074/jbc.M111977200. PMID 11790796.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Clark HF, Gurney AL, Abaya E, et al. (2003). "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment". Genome Res. 13 (10): 2265–70. doi:10.1101/gr.1293003. PMC 403697. PMID 12975309.
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
  • Abe A, Poucher HK, Hiraoka M, Shayman JA (2004). "Induction of lysosomal phospholipase A2 through the retinoid X receptor in THP-1 cells". J. Lipid Res. 45 (4): 667–73. doi:10.1194/jlr.M300342-JLR200. PMID 14754907.
  • Zhang Z, Henzel WJ (2005). "Signal peptide prediction based on analysis of experimentally verified cleavage sites". Protein Sci. 13 (10): 2819–24. doi:10.1110/ps.04682504. PMC 2286551. PMID 15340161.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Otsuki T, Ota T, Nishikawa T, et al. (2007). "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries". DNA Res. 12 (2): 117–26. doi:10.1093/dnares/12.2.117. PMID 16303743.


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